On the public citation graph

Effective Screening Strategy Using Ensembled Pharmacophore Models Combined with Cascade Docking: Application to p53-MDM2 Interaction Inhibitors

https://doi.org/10.1021/ci400348f
0 signed · 81 inferred · view as graph

Inferred edges come from two machine sources: sweeps of open repository metadata (mostly SSRN and Zenodo), and a bulk OpenAlex citation snapshot. Every row below is labelled with the one it came from. Neither is a complete citation index — absence here is not evidence of absence.

Is this your work? Sign in with ORCID and put your name on the claims that are yours.
Claim with ORCID
Reference health. See whether every reference in this work resolves to a known work and none has been retracted — and get a dated CiteStamped badge you can embed.
See reference health

What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/anie.201003863openalex-snapshot
The Structure‐Based Design of Mdm2/Mdmx–p53 Inhibitors Gets Serious
inferredcites →https://doi.org/10.1002/prot.1136openalex-snapshot
QSAR: Hydropathic analysis of inhibitors of the p53–mdm2 interaction
inferredcites →https://doi.org/10.1007/978-1-62703-236-0_8openalex-snapshot
Identification of Small Molecules Affecting p53-MDM2/MDMX Interaction by Fluorescence Polarization
inferredcites →https://doi.org/10.1007/bf00124387openalex-snapshot
The computer program LUDI: A new method for the de novo design of enzyme inhibitors
inferredcites →https://doi.org/10.1007/s10969-007-9027-2openalex-snapshot
The scientific impact of the Structural Genomics Consortium: a protein family and ligand-centered approach to medically-relevant human proteins
inferredcites →https://doi.org/10.1016/0092-8674(93)90132-aopenalex-snapshot
Crystal structure of the soluble human 55 kd TNF receptor-human TNFβ complex: Implications for TNF receptor activation
inferredcites →https://doi.org/10.1016/j.ab.2004.03.009openalex-snapshot
Fluorescence polarization assay and inhibitor design for MDM2/p53 interaction
inferredcites →https://doi.org/10.1016/j.ab.2004.05.055openalex-snapshot
Development and optimization of a binding assay for the XIAP BIR3 domain using fluorescence polarization
inferredcites →https://doi.org/10.1016/j.bbrc.2012.06.138openalex-snapshot
Molecular dynamics studies on Mdm2 complexes: An analysis of the inhibitor influence
inferredcites →https://doi.org/10.1016/j.bmcl.2009.04.124openalex-snapshot
Identification of a disruptor of the MDM2-p53 protein–protein interaction facilitated by high-throughput in silico docking
inferredcites →https://doi.org/10.1016/j.cbpa.2011.05.024openalex-snapshot
Chemical and structural lessons from recent successes in protein–protein interaction inhibition (2P2I)
inferredcites →https://doi.org/10.1016/j.drudis.2009.11.007openalex-snapshot
Rationalizing the chemical space of protein–protein interaction inhibitors
inferredcites →https://doi.org/10.1016/j.semcancer.2009.10.003openalex-snapshot
Small-molecule inhibitors of MDM2 as new anticancer therapeutics
inferredcites →https://doi.org/10.1016/s0003-2697(04)00223-4openalex-snapshot
Fluorescence polarization assay and inhibitor design for MDM2/p53 interaction
inferredcites →https://doi.org/10.1016/s0169-409x(00)00129-0openalex-snapshot
Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings 1PII of original article: S0169-409X(96)00423-1. The article was originally published in Advanced Drug Delivery Reviews 23 (1997) 3–25. 1
inferredcites →https://doi.org/10.1016/s1359-6446(03)02831-9openalex-snapshot
A ‘Rule of Three’ for fragment-based lead discovery?
inferredcites →https://doi.org/10.1021/cc050142vopenalex-snapshot
Proteomimetic Libraries: Design, Synthesis, and Evaluation of p53−MDM2 Interaction Inhibitors
inferredcites →https://doi.org/10.1021/ci049885eopenalex-snapshot
LigandScout: 3-D Pharmacophores Derived from Protein-Bound Ligands and Their Use as Virtual Screening Filters
inferredcites →https://doi.org/10.1021/ci100113popenalex-snapshot
Molecular Interaction Fields and 3D-QSAR Studies of p53−MDM2 Inhibitors Suggest Additional Features of Ligand−Target Interaction
inferredcites →https://doi.org/10.1021/ci200280mopenalex-snapshot
Discovery of Novel Selective Serotonin Reuptake Inhibitors through Development of a Protein-Based Pharmacophore
inferredcites →https://doi.org/10.1021/ci200620hopenalex-snapshot
Protein Pharmacophore Selection Using Hydration-Site Analysis
inferredcites →https://doi.org/10.1021/ci300112jopenalex-snapshot
ADMET Evaluation in Drug Discovery. 11. PharmacoKinetics Knowledge Base (PKKB): A Comprehensive Database of Pharmacokinetic and Toxic Properties for Drugs
inferredcites →https://doi.org/10.1021/ci300367aopenalex-snapshot
admetSAR: A Comprehensive Source and Free Tool for Assessment of Chemical ADMET Properties
inferredcites →https://doi.org/10.1021/ci4000745openalex-snapshot
Enrichment Factor Analyses on G-Protein Coupled Receptors with Known Crystal Structure
inferredcites →https://doi.org/10.1021/ci900345hopenalex-snapshot
Ligand−Protein Cross-Docking with Water Molecules
inferredcites →https://doi.org/10.1021/ja073687xopenalex-snapshot
Small Molecule Inhibitors of the MDM2-p53 Interaction Discovered by Ensemble-Based Receptor Models
inferredcites →https://doi.org/10.1021/ja800201jopenalex-snapshot
Quantitative Lid Dynamics of MDM2 Reveals Differential Ligand Binding Modes of the p53-Binding Cleft
inferredcites →https://doi.org/10.1021/jm049137gopenalex-snapshot
Discovery and Cocrystal Structure of Benzodiazepinedione HDM2 Antagonists That Activate p53 in Cells
inferredcites →https://doi.org/10.1021/jm060023+openalex-snapshot
Discovery of a Nanomolar Inhibitor of the Human Murine Double Minute 2 (MDM2)−p53 Interaction through an Integrated, Virtual Database Screening Strategy
inferredcites →https://doi.org/10.1021/jm200045vopenalex-snapshot
Small-Molecule Ligands of Methyl-Lysine Binding Proteins
inferredcites →https://doi.org/10.1021/jm3007068openalex-snapshot
AM-8553: A Novel MDM2 Inhibitor with a Promising Outlook for Potential Clinical Development
inferredcites →https://doi.org/10.1021/jm300969topenalex-snapshot
Discovery, Synthesis, and Biological Evaluation of Orally Active Pyrrolidone Derivatives as Novel Inhibitors of p53–MDM2 Protein–Protein Interaction
inferredcites →https://doi.org/10.1021/jm900681hopenalex-snapshot
Discovery and Optimization of Chromenotriazolopyrimidines as Potent Inhibitors of the Mouse Double Minute 2−Tumor Protein 53 Protein−Protein Interaction
inferredcites →https://doi.org/10.1021/jm901400zopenalex-snapshot
Potent and Orally Active Small-Molecule Inhibitors of the MDM2−p53 Interaction
inferredcites →https://doi.org/10.1021/ml4000657openalex-snapshot
Discovery of RG7112: A Small-Molecule MDM2 Inhibitor in Clinical Development
inferredcites →https://doi.org/10.1038/35050012openalex-snapshot
Structural basis of IAP recognition by Smac/DIABLO
inferredcites →https://doi.org/10.1038/nature06526openalex-snapshot
Reaching for high-hanging fruit in drug discovery at protein–protein interfaces
inferredcites →https://doi.org/10.1038/nrc991openalex-snapshot
Inhibiting the p53–MDM2 interaction: an important target for cancer therapy
inferredcites →https://doi.org/10.1039/b211889kopenalex-snapshot
Binding of an inhibitor of the p53/MDM2 Interaction to MDM2
inferredcites →https://doi.org/10.1073/pnas.1203789109openalex-snapshot
Activation of the p53 pathway by small-molecule-induced MDM2 and MDMX dimerization
inferredcites →https://doi.org/10.1093/emboj/19.13.3179openalex-snapshot
The bacterial cell‐division protein ZipA and its interaction with an FtsZ fragment revealed by X‐ray crystallography
inferredcites →https://doi.org/10.1093/protein/gzm083openalex-snapshot
LOOPER: a molecular mechanics-based algorithm for protein loop prediction
inferredcites →https://doi.org/10.1110/ps.036335.108openalex-snapshot
A fast and accurate computational approach to protein ionization
inferredcites →https://doi.org/10.1126/science.1092472openalex-snapshot
In Vivo Activation of the p53 Pathway by Small-Molecule Antagonists of MDM2
inferredcites →https://doi.org/10.1126/science.274.5289.948openalex-snapshot
Structure of the MDM2 Oncoprotein Bound to the p53 Tumor Suppressor Transactivation Domain
inferredcites →https://doi.org/10.1126/science.275.5302.983openalex-snapshot
Structure of Bcl-x L -Bak Peptide Complex: Recognition Between Regulators of Apoptosis
inferredcites →https://doi.org/10.1158/1535-7163.mct-10-0337openalex-snapshot
The Novel Tryptamine Derivative JNJ-26854165 Induces Wild-Type p53- and E2F1-Mediated Apoptosis in Acute Myeloid and Lymphoid Leukemias
inferredcites →https://doi.org/10.1371/journal.pone.0040897openalex-snapshot
Simulating Molecular Mechanisms of the MDM2-Mediated Regulatory Interactions: A Conformational Selection Model of the MDM2 Lid Dynamics
inferredcites →https://doi.org/10.2174/092986710792232021openalex-snapshot
Molecular Modeling Approaches in the Discovery of New Drugs for Anti-Cancer Therapy: The Investigation of p53-MDM2 Interaction and its Inhibition by Small Molecules
inferredcites →https://doi.org/10.2174/156802607779318325openalex-snapshot
Modulation of Protein-Protein Interactions by Stabilizing/Mimicking Protein Secondary Structure Elements
inferredcites →https://doi.org/10.4161/cc.8.8.8185openalex-snapshot
High affinity interaction of the p53 peptide-analogue with human Mdm2 and Mdmx
inferredcites →https://doi.org/10.4161/cc.9.6.10956openalex-snapshot
Structures of low molecular weight inhibitors bound to MDMX and MDM2 reveal new approaches for p53-MDMX/MDM2 antagonist drug discovery

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

inferred← citeshttps://doi.org/10.1002/cjoc.201800552openalex-snapshot
Drug Design of “Undruggable” Targets
inferred← citeshttps://doi.org/10.1002/jmr.2471openalex-snapshot
Improvements, trends, and new ideas in molecular docking: 2012–2013 in review
inferred← citeshttps://doi.org/10.1002/med.21393openalex-snapshot
Medicinal Chemistry Strategies to Disrupt the p53–MDM2/MDMX Interaction
inferred← citeshttps://doi.org/10.1007/978-981-13-0773-7_4openalex-snapshot
Computational Methods Applicable to the Discovery of Small-Molecule Inhibitors of Protein-Protein Interactions
inferred← citeshttps://doi.org/10.1007/s00044-017-1788-yopenalex-snapshot
Identification of novel MEK1 inhibitors by pharmacophore and docking based virtual screening
inferred← citeshttps://doi.org/10.1007/s10822-017-0028-3openalex-snapshot
Multiple receptor-ligand based pharmacophore modeling and molecular docking to screen the selective inhibitors of matrix metalloproteinase-9 from natural products
inferred← citeshttps://doi.org/10.1016/j.bmc.2021.116530openalex-snapshot
A computer-aided drug design approach to discover tumour suppressor p53 protein activators for colorectal cancer therapy
inferred← citeshttps://doi.org/10.1016/j.compbiolchem.2018.02.004openalex-snapshot
Scaffold-based novel SHP2 allosteric inhibitors design using Receptor-Ligand pharmacophore model, virtual screening and molecular dynamics
inferred← citeshttps://doi.org/10.1016/j.molstruc.2021.131399openalex-snapshot
Discovery of potent HDAC2 inhibitors based on virtual screening in combination with drug repurposing
inferred← citeshttps://doi.org/10.1016/j.ymeth.2014.07.007openalex-snapshot
Hierarchical virtual screening approaches in small molecule drug discovery
inferred← citeshttps://doi.org/10.1016/j.ymeth.2017.08.006openalex-snapshot
In silico structure-based approaches to discover protein-protein interaction-targeting drugs
inferred← citeshttps://doi.org/10.1021/acs.biochem.7b00085openalex-snapshot
A Fusion Protein of the p53 Transaction Domain and the p53-Binding Domain of the Oncoprotein MdmX as an Efficient System for High-Throughput Screening of MdmX Inhibitors
inferred← citeshttps://doi.org/10.1021/acs.jcim.5b00747openalex-snapshot
An Effective Virtual Screening Protocol To Identify Promising p53–MDM2 Inhibitors
inferred← citeshttps://doi.org/10.1021/acs.jcim.7b00017openalex-snapshot
Protein–Ligand Empirical Interaction Components for Virtual Screening
inferred← citeshttps://doi.org/10.1021/jm500692uopenalex-snapshot
Fast Identification of Novel Lymphoid Tyrosine Phosphatase Inhibitors Using Target–Ligand Interaction-Based Virtual Screening
inferred← citeshttps://doi.org/10.1039/c4md00328dopenalex-snapshot
Rational design of protein–protein interaction inhibitors
inferred← citeshttps://doi.org/10.1039/d0ra01483dopenalex-snapshot
Developing an effective polarizable bond method for small molecules with application to optimized molecular docking
inferred← citeshttps://doi.org/10.1080/07391102.2018.1434833openalex-snapshot
Hierarchical virtual screening of the dual MMP-2/HDAC-6 inhibitors from natural products based on pharmacophore models and molecular docking
inferred← citeshttps://doi.org/10.2174/0929867330666221114103924openalex-snapshot
Recent Advancements in the Discovery of MDM2/MDM2-p53 Interaction Inhibitors for the Treatment of Cancer
inferred← citeshttps://doi.org/10.3390/molecules23123174openalex-snapshot
An Application of Fit Quality to Screen MDM2/p53 Protein-Protein Interaction Inhibitors
inferred← citeshttps://doi.org/10.4155/fmc-2017-0127openalex-snapshot
Virtual Screening and Biological Evaluation of Biofilm Inhibitors on Dual Targets in Quorum Sensing System
inferred← citeshttps://doi.org/10.70675/9ab04dcaz498fz43ebz8762z012f3f86154copenalex-snapshot
A yeast-based assay to screen protein-protein interaction modulators
inferred← citeshttps://doi.org/10.7287/peerj.8620v0.1/reviews/1openalex-snapshot
Peer Review #1 of "Discovery of potential targets of Triptolide through inverse docking in ovarian cancer cells (v0.1)"
inferred← citeshttps://doi.org/10.7287/peerj.8620v0.1/reviews/2openalex-snapshot
Peer Review #2 of "Discovery of potential targets of Triptolide through inverse docking in ovarian cancer cells (v0.1)"
inferred← citeshttps://doi.org/10.7287/peerj.8620v0.1/reviews/3openalex-snapshot
Peer Review #3 of "Discovery of potential targets of Triptolide through inverse docking in ovarian cancer cells (v0.1)"
inferred← citeshttps://doi.org/10.7287/peerj.8620v0.2/reviews/1openalex-snapshot
Peer Review #1 of "Discovery of potential targets of Triptolide through inverse docking in ovarian cancer cells (v0.2)"
inferred← citeshttps://doi.org/10.7287/peerj.8620v0.2/reviews/2openalex-snapshot
Peer Review #2 of "Discovery of potential targets of Triptolide through inverse docking in ovarian cancer cells (v0.2)"
inferred← citeshttps://doi.org/10.7717/peerj.2757openalex-snapshot
Discovery of novel inhibitors disrupting HIF-1α/von Hippel–Lindau interaction through shape-based screening and cascade docking
inferred← citeshttps://doi.org/10.7717/peerj.8620openalex-snapshot
Discovery of potential targets of Triptolide through inverse docking in ovarian cancer cells
Editorial review for independent work. ICSAC — the Institute for Complexity Science and Advanced Computing — runs a structured editorial panel for researchers publishing outside journals, and publishes on CiteStamp rails. Submission is free and goes through ORCID: icsacinstitute.org/submit.